PDBsum entry: 2bud

Transferase

PDB id: 2bud

Contents

Protein chain

92 a.a. *

* Residue conservation analysis

PDB id:

2bud

Name:

Transferase

Title:

The solution structure of the chromo barrel domain from the males-absent on the first (mof) protein

Structure:

Males-absent on the first protein. Chain: a. Fragment: chromo barrel domain, residues 367-454. Synonym: putative acetyl transferase mof. Engineered: yes

Source:

Drosophila melanogaster. Fruit fly. Organism_taxid: 7227. Expressed in: escherichia coli. Expression_system_taxid: 511693. Expression_system_variant: tuner(de3) placi.

NMR struc:

25 models

Authors:

P.R.Nielsen,D.Nietlispach,A.Buscaino,R.J.Warner,A.Akhtar, A.G.Murzin,N.V.Murzina,E.D.Laue

Key ref:

P.R.Nielsen et al. (2005). Structure of the chromo barrel domain from the MOF acetyltransferase. J Biol Chem, 280, 32326-32331. PubMed id: 15964847 DOI: 10.1074/jbc.M501347200

Date:

09-Jun-05 Release date: 24-Jun-05

Protein chain

O02193  (MOF_DROME) -  Males-absent on the first protein

Seq: 827 a.a.

Struc: 92 a.a.*

* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 

• Cellular component: nucleus (2 terms)
• Biological process: chromatin assembly or disassembly (1 term)
• Biochemical function: chromatin binding (1 term)

DOI no: 10.1074/jbc.M501347200

J Biol Chem 280:32326-32331 (2005)

PubMed id: 15964847

Structure of the chromo barrel domain from the MOF acetyltransferase.

P.R.Nielsen, D.Nietlispach, A.Buscaino, R.J.Warner, A.Akhtar, A.G.Murzin, N.V.Murzina, E.D.Laue.

ABSTRACT

We report here the structure of the putative chromo domain from MOF, a member of the MYST family of histone acetyltransferases that acetylates histone H4 at Lys-16 and is part of the dosage compensation complex in Drosophila. We found that the structure of this domain is a beta-barrel that is distinct from the alpha + beta fold of the canonical chromo domain. Despite the differences, there are similarities that support an evolutionary relationship between the two domains, and we propose the name "chromo barrel." The chromo barrel domains may be divided into two groups, MSL3-like and MOF-like, on the basis of whether a group of conserved aromatic residues is present or not. The structure suggests that, although the MOF-like domains may have a role in RNA binding, the MSL3-like domains could instead bind methylated residues. The MOF chromo barrel shares a common fold with other chromatin-associated modules, including the MBT-like repeat, Tudor, and PWWP domains. This structural similarity suggests a probable evolutionary pathway from these other modules to the canonical chromo domains (or vice versa) with the chromo barrel domain representing an intermediate structure.

Selected figure(s)

Figure 3.
FIGURE 3. Comparison of the structures of the MOF chromo barrel and the HP1 chromo domain-histone H3 peptide complex. a, superposition (using residues in the -strands) of the MOF chromo barrel and the HP1 chromo domain (residues 17-75)-histone H3 peptide (residues 4-11) complex. b, close up view of the methyl lysine binding site in a (where the structures are now superimposed using residues in the aromatic site) showing the three residues that form the aromatic pocket. Side chains from the MOF domain are shown in blue, from the HP1 chromo domain, in red, and from histone H3, in yellow. N, N terminus; C, C terminus.

Figure 4.
FIGURE 4. The family of structures related to the chromo domain. The five strands in the MOF chromo barrel are color coded as in Fig. 2 with the remainder of the backbone in gray, apart from the loop connecting strands 2 and 3, which is yellow. In the HP1 chromo domain-histone H3 complex, the H3 peptide is black, and the methyl-K9 is purple. In the HP1 chromo shadow domain-CAF-1 p150 complex, one of the monomers is shaded in softer tones, and the CAF-1 peptide is pink. Sso7 is also shown in its complex with DNA. Strands that are equivalent to those in the MOF chromo barrel are shown using the same color scheme, and the positions of the conserved aromatic residues are indicated by spheres. The Protein Data Bank accession numbers for the structures used in the Fig. are as follows: MBT domain, 1oi1; Tudor domain, 1mhn; HP1 chromo domain-histone H3 complex, 1guw; HP1 chromo shadow domain-CAF-1 p150 complex, 1s4z; and the Sso7-DNA complex, 1bf4.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2005, 280, 32326-32331) copyright 2005.

Figures were selected by an automated process.